One third of all cancer therapeutics in clinical trials today are monoclonal antibodies (MAbs). Mab purification is traditionally performed using affinity and ion-chromatography. The media, however, is expensive (>$100,000/L) and unstable at room-temperature. Lynntech, Inc. proposes to develop inexpensive MAb-affinity beads for purifying cancer therapeutic monoclonal antibodies which will be as equally effective as Protein A beads. Lynntech's MAb-affinity beads will exhibit shape and size exclusive binding properties formed during their synthesis, whereby a process of monomer self-assembly occurs forming spatial arrangements of functional monomers which are frozen in space via polymer propagation around the MAb template. The network of functionalized polymers form pockets of specific size and shape character for which MAb rebinds with broad MAb selectivity will allow for high levels of MAb purification at minimal costs, due to the inexpensive materials used for their synthesis and the ability to recycle MAb for several rounds of MAb-affinity bead synthesis cycles. The anticipated benefit from developing inexpensive MAb-affinity beads will be immediately appreciated when the reduced costs of purifying cancer therapeutic antibodies results in an increased therapeutic antibody manufacturer profit and a reduction in medical costs) passed along to the consumers. IgG-affinity beads have already been synthesized and characterized for their IgG binding and recovery capacity which were 0.65mg/mL and >99%, respectively, during non-optimized preliminary studies. During the Phase I, MAb-affinity beads will be synthesized and carefully analyzed for their MAb binding and recovery capacity in affinity column chromatography experiments. Comparison will be made between the purification properties of Lynntech's MAb-affinity beads, Protein A and control beads in the form of BSA-affinity beads prepared in the same manner as MAb-affinity beads.